Research workbench
AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase heme-binding subunit msrq (A6VCE4)
Analyse AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6VCE4
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd92eb9B6Bd45d2c5FBB3651b469A6CA52af64a1D
- Molecule
- Protein-methionine-sulfoxide reductase heme-binding subunit msrq
- UniProt
- A6VCE4
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-methionine-sulfoxide reductase heme-binding subunit msrq | protein | 202 | 78% helix, 0% strand | A6VCE4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.76 | 0.87 | 43 | empty |
| 2 | 216 | 0.65 | 0.83 | 26 | empty |
| 3 | 57 | 0.29 | 0.74 | 19 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A6VCE4
- Elsewhere: UniProt A6VCE4 · AlphaFold DB A6VCE4
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